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HSP90_THEPA
ID   HSP90_THEPA             Reviewed;         721 AA.
AC   P24724; Q4N5P6;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 2.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Heat shock protein 90;
DE            Short=HSP90;
GN   OrderedLocusNames=TP02_0244;
OS   Theileria parva (East coast fever infection agent).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Theileriidae; Theileria.
OX   NCBI_TaxID=5875;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Gerhards J., Morzarin S.P., Musoke A.J., Lipp J., Williams R.O.;
RT   "Sequence and expression of a 90 kilodalton heat-shock protein.";
RL   Submitted (FEB-1991) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Muguga;
RX   PubMed=15994558; DOI=10.1126/science.1110439;
RA   Gardner M.J., Bishop R., Shah T., de Villiers E.P., Carlton J.M., Hall N.,
RA   Ren Q., Paulsen I.T., Pain A., Berriman M., Wilson R.J.M., Sato S.,
RA   Ralph S.A., Mann D.J., Xiong Z., Shallom S.J., Weidman J., Jiang L.,
RA   Lynn J., Weaver B., Shoaibi A., Domingo A.R., Wasawo D., Crabtree J.,
RA   Wortman J.R., Haas B., Angiuoli S.V., Creasy T.H., Lu C., Suh B.,
RA   Silva J.C., Utterback T.R., Feldblyum T.V., Pertea M., Allen J.,
RA   Nierman W.C., Taracha E.L.N., Salzberg S.L., White O.R., Fitzhugh H.A.,
RA   Morzaria S., Venter J.C., Fraser C.M., Nene V.;
RT   "Genome sequence of Theileria parva, a bovine pathogen that transforms
RT   lymphocytes.";
RL   Science 309:134-137(2005).
CC   -!- FUNCTION: Molecular chaperone that promotes the maturation, structural
CC       maintenance and proper regulation of specific target proteins involved
CC       for instance in cell cycle control and signal transduction. Undergoes a
CC       functional cycle that is linked to its ATPase activity. This cycle
CC       probably induces conformational changes in the client proteins, thereby
CC       causing their activation. Interacts dynamically with various co-
CC       chaperones that modulate its substrate recognition, ATPase cycle and
CC       chaperone function (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DOMAIN: The TPR repeat-binding motif mediates interaction with TPR
CC       repeat-containing proteins. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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DR   EMBL; M57386; AAA30132.1; -; mRNA.
DR   EMBL; AAGK01000002; EAN32527.1; -; Genomic_DNA.
DR   RefSeq; XP_764810.1; XM_759717.1.
DR   AlphaFoldDB; P24724; -.
DR   SMR; P24724; -.
DR   STRING; 5875.XP_764810.1; -.
DR   PRIDE; P24724; -.
DR   EnsemblProtists; EAN32527; EAN32527; TP02_0244.
DR   GeneID; 3501902; -.
DR   KEGG; tpv:TP02_0244; -.
DR   VEuPathDB; PiroplasmaDB:TpMuguga_02g00244; -.
DR   eggNOG; KOG0019; Eukaryota.
DR   InParanoid; P24724; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000001949; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   Gene3D; 1.20.120.790; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   HAMAP; MF_00505; HSP90; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR019805; Heat_shock_protein_90_CS.
DR   InterPro; IPR037196; HSP90_C.
DR   InterPro; IPR001404; Hsp90_fam.
DR   InterPro; IPR020575; Hsp90_N.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   PANTHER; PTHR11528; PTHR11528; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF110942; SSF110942; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS00298; HSP90; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW   Stress response.
FT   CHAIN           1..721
FT                   /note="Heat shock protein 90"
FT                   /id="PRO_0000062943"
FT   REGION          219..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          697..721
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           717..721
FT                   /note="TPR repeat-binding"
FT   COMPBIAS        235..269
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         44
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         86
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         131
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         395
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        508
FT                   /note="A -> S (in Ref. 1; AAA30132)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   721 AA;  83668 MW;  A745C2B3B50ED924 CRC64;
     MTSKDETPDQ EVYAFNADIS QLLSLIINAF YSNKEIFLRE LISNASDALE KIRYEAIKDP
     KQIEDQPDYY IRLYADKNNN TLTIEDSGIG MTKADLVNNL GTIAKSGTRA FMEALQAGSD
     MSMIGQFGVG FYSAYLVADK VTVVSKNNAD DQYVWESTAS GHFTVKKDDS HEPLKRGTRL
     ILHLKEDQTE YLEERRLKEL VKKHSEFISF PISLSVEKTQ ETEVTDDEAE LDEDKKPEEE
     KPKDDKVEDV TDEKVTDVTD EEEKKEEKKK KKRKVTNVTR EWEMLNKQKP IWMRLPSEVT
     NEEYAAFYKN LTNDWEDHLA VKHFSVEGQL EFKALLFVPR RAPFDMFESR KKKNNIKLYV
     RRVFIMDDCE ELIPEWLSFV KGVVDSEDLP LNISRETLQQ NKILKVIRKN LVKKCLELFN
     ELTEKKEDFK KFYEQFSKNL KLGIHEDNAN RSKIAELLRF ETTKSGDELV SLKEYVDRMK
     SDQKYVYYIT GESKQSVASS PFLETLRARD YEVLYMTDPI DEYAVQQIKE FEGKKLKCCT
     KEGLDLDEGE DEKKSFEALK EEMEPLCKHI KEVLHDKVEK VVCGTRFTDS PCALVTSEFG
     WSANMERIMK AQALRDSSIT SYMLSKKIME INPRHSIMKE LKTRAANDKT DKTVKDLVWL
     LYDTALLTSG FNLDEPTQFG NRIYRMIKLG LSLDDEEHVE EDSSMPPLDE PVVDSKMEEV
     D
 
 
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